1pve

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[[Image:1pve.jpg|left|200px]]
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{{Structure
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|GENE= HH23B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1pve| PDB=1pve | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pve OCA], [http://www.ebi.ac.uk/pdbsum/1pve PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pve RCSB]</span>
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'''Solution structure of XPC binding domain of hHR23B'''
'''Solution structure of XPC binding domain of hHR23B'''
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[[Category: Kim, H J.]]
[[Category: Kim, H J.]]
[[Category: Ryu, K S.]]
[[Category: Ryu, K S.]]
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[[Category: Chap]]
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[[Category: hhr23b]]
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[[Category: Hhr23b]]
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[[Category: nmr solution structure]]
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[[Category: Nmr solution structure]]
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[[Category: nucleotide excision repair]]
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[[Category: Nucleotide excision repair]]
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[[Category: xpc binding domain]]
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[[Category: Xpc binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:31:52 2008''
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Revision as of 02:31, 3 May 2008

Template:STRUCTURE 1pve

Solution structure of XPC binding domain of hHR23B


Overview

Human cells contain two homologs of the yeast RAD23 protein, hHR23A and hHR23B, which participate in the DNA repair process. hHR23B houses a domain (residues 277-332, called XPCB) that binds specifically and directly to the xeroderma pigmentosum group C protein (XPC) to initiate nucleotide excision repair (NER). This domain shares sequence homology with a heat shock chaperonin-binding motif that is also found in the stress-inducible yeast phosphoprotein STI1. We determined the solution structure of a protein fragment containing amino acids 275-342 of hHR23B (termed XPCB-hHR23B) and compared it with the previously reported solution structures of the corresponding domain of hHR23A. The periodic positioning of proline residues in XPCB-hHR23B produced kinked alpha helices and assisted in the formation of a compact domain. Although the overall structure of the XPCB domain was similar in both XPCB-hHR23B and XPCB-hHR23A, the N-terminal part (residues 275-283) of XPCB-hHR23B was more flexible than the corresponding part of hHR23A. We tried to infer the characteristics of this flexibility through (15)N-relaxation studies. The hydrophobic surface of XPCB-hHR23B, which results from the diverse distribution of N-terminal region, might give rise to the functional pleiotropy observed in vivo for hHR23B, but not for hHR23A.

About this Structure

1PVE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B., Kim B, Ryu KS, Kim HJ, Cho SJ, Choi BS, FEBS J. 2005 May;272(10):2467-76. PMID:15885096 Page seeded by OCA on Sat May 3 05:31:52 2008

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